ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural analysis of human Cdc20 supports multisite degron recognition by APC/C.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed.
- BubR1 TPR domain supports the mitotic checkpoint by promoting MCC formation and MCC-APC/C interaction.Communications biology · 2026Article
- Multimodal integration of pathomics and single-cell transcriptomics reveals CDC20 as a link between prostate cancer recurrence and benzo[a]pyrene-responsive phenotypes.Frontiers in cell and developmental biology · 2026Article
- Article
- Proteasome-derived peptides: separating the trash from the recycling.Trends in biochemical sciences · 2025Review
- Proteolysis-targeting influenza vaccine strains induce broad-spectrum immunity and in vivo protection.Nature microbiology · 2025Article
- Emerging Roles of PTTG1/Securin in Breast Cancer.Journal of Cancer · 2025Review
- Production of SAC Proteins in a Baculovirus-Based Heterologous Gene Expression System.Methods in molecular biology (Clifton, N.J.) · 2025Article
- CDC20 and CCNB1 Overexpression as Prognostic Markers in Bladder Cancer.Diagnostics (Basel, Switzerland) · 2024Article
- The Tumor Suppressor TPD52-Governed Endoplasmic Reticulum Stress is Modulated by APCAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A comparative study of the cryo-EM structures ofeLife · 2024Article
- Functional analysis of Cdc20 reveals a critical role of CRY box in mitotic checkpoint signaling.Communications biology · 2024Article
- Discovery of New Binders for DCAF1, an Emerging Ligase Target in the Targeted Protein Degradation Field.ACS medicinal chemistry letters · 2023Article
- Kinetochore-catalyzed MCC formation: A structural perspective.IUBMB life · 2023Article
- The structural flexibility of MAD1 facilitates the assembly of the Mitotic Checkpoint Complex.Nature communications · 2023Article
- Discovery of Ureido-Based Apcin Analogues as Cdc20-specific Inhibitors against Cancer.Pharmaceuticals (Basel, Switzerland) · 2023Article
- CDC20 in and out of mitosis: a prognostic factor and therapeutic target in hematological malignancies.Journal of experimental & clinical cancer research : CR · 2022Review
- Design, Synthesis, and Biological Evaluation of Apcin-Based CDC20 Inhibitors.ACS medicinal chemistry letters · 2022Article
- Biochemical, biophysical, and functional characterisation of the E3 ubiquitin ligase APC/C regulator CDC20 fromFrontiers in physiology · 2022Article
- A prometaphase mechanism of securin destruction is essential for meiotic progression in mouse oocytes.Nature communications · 2021Article
- E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones.SLAS discovery : advancing life sciences R & D · 2021Review
8 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
The anaphase-promoting complex/cyclosome (APC/C) promotes anaphase onset and mitotic exit through ubiquitinating securin and cyclin B1. The mitotic APC/C activator, the cell division cycle 20 (Cdc20) protein, directly interacts with APC/C degrons--the destruction (D) and KEN boxes. APC/C(Cdc20) is the target of the spindle checkpoint. Checkpoint inhibition of APC/C(Cdc20) requires the binding of a BubR1 KEN box to Cdc20. How APC/C recognizes substrates is not understood. We report the crystal structures of human Cdc20 alone or bound to a BubR1 KEN box. Cdc20 has a disordered N-terminal region and a C-terminal WD40 β propeller with a preformed KEN-box-binding site at its top face. We identify a second conserved surface at the side of the Cdc20 β propeller as a D-box-binding site. The D box of securin, but not its KEN box, is critical for securin ubiquitination by APC/C(Cdc20). Although both motifs contribute to securin ubiquitination by APC/C(Cdh1), securin mutants lacking either motif are efficiently ubiquitinated. Furthermore, D-box peptides diminish the ubiquitination of KEN-box substrates by APC/C(Cdh1), suggesting possible competition between the two motifs. Our results indicate the lack of strong positive cooperativity between the two degrons of securin. We propose that low-cooperativity, multisite target recognition enables APC/C to robustly ubiquitinate diverse substrates and helps to drive cell cycle oscillations.
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